NAK1_SCHPO
ID NAK1_SCHPO Reviewed; 652 AA.
AC O75011;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Serine/threonine-protein kinase nak1;
DE EC=2.7.11.1;
DE AltName: Full=N-rich kinase 1;
GN Name=nak1; ORFNames=SPBC17F3.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12427731; DOI=10.1074/jbc.m208993200;
RA Huang T.Y., Markley N.A., Young D.;
RT "Nak1, an essential GC kinase regulates cell morphology and growth in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 278:991-997(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in the regulation of cell polarity, growth and
CC division. {ECO:0000269|PubMed:12427731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427731}.
CC -!- PTM: Autophosphorylated. {ECO:0000305|PubMed:18257517}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF091345; AAC63343.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20324.1; -; Genomic_DNA.
DR PIR; T39722; T39722.
DR RefSeq; NP_596023.1; NM_001021931.2.
DR AlphaFoldDB; O75011; -.
DR SMR; O75011; -.
DR BioGRID; 276507; 16.
DR STRING; 4896.SPBC17F3.02.1; -.
DR iPTMnet; O75011; -.
DR SwissPalm; O75011; -.
DR MaxQB; O75011; -.
DR PaxDb; O75011; -.
DR PRIDE; O75011; -.
DR EnsemblFungi; SPBC17F3.02.1; SPBC17F3.02.1:pep; SPBC17F3.02.
DR GeneID; 2539963; -.
DR KEGG; spo:SPBC17F3.02; -.
DR PomBase; SPBC17F3.02; nak1.
DR VEuPathDB; FungiDB:SPBC17F3.02; -.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O75011; -.
DR OMA; YEFGEAN; -.
DR PhylomeDB; O75011; -.
DR Reactome; R-SPO-75153; Apoptotic execution phase.
DR PRO; PR:O75011; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0071958; C:new mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:PomBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:2000247; P:positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0071574; P:protein localization to medial cortex; IDA:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0062200; P:RAM/MOR signaling pathway; NAS:PomBase.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..652
FT /note="Serine/threonine-protein kinase nak1"
FT /id="PRO_0000086416"
FT DOMAIN 10..264
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 652 AA; 71120 MW; 472BB9721B1F2E09 CRC64;
MENNTASSPY TKLELVGRGS YGAVYRGICN LTKETVAIKI LNLDTDEDEV SDIQKEVAVL
SELKQSDVEN IIKYHGSYLV GTNLWIIMDY CHGGSVRTLM EAGPISEPCI SLILRETLQA
LKFIHHAGII HRDIKAANIL VSMSGNVKLC DFGVAAELNI NRRKRITFIG TPYWMAPEVI
RDGQEYNVMA DIWSLGITAY EIATGSPPHA KEDPFRAVYL IAHTAPPRLN GNFSALLKEF
IASCLQDVPQ RRLDSSELLK SKFIKQYSRM SISELTNVVK RYDTWQAAGG IPQTLLLGEE
ADDGSDPDQE TSDTAASDDG WEFGTIKQGQ SNVSSITGTS TSTTTAATSS TTVTGTVIPK
SSTVHEPPSS NDSHPLLQLF KDSKISDDDS PSNAEGASTE DSKGEVSYSQ IELPSLDSSN
LSSKKSTIQS KHTKQAEDYD LFVGRTRSNS KTSSDQSIKR PLPRVVQRQK TSLGKRGISM
SPMKPGLRMP SSFDLQSRSI SMGAFEQLST PLEAPAHKHS AVLQPLEVNR SISIPPPKSI
SPSILHKPSL ESASSTPKIS SCSSTPKPFN SKLRAHLPPL SIGSPAVQPL ANDNYDSLGV
RGLNMELFND YPGNMHNIKS VLSLEIDIVL GEMDACLKSL ECNLLNRKAY NE
